SPINT2 Human, Sf9

SPINT2 contains two extracellular Kunitz domains that are responsible for its inhibitory activity against serine proteases . These domains allow SPINT2 to inhibit plasmin, plasma and tissue kallikrein, and factor XIa . One of the key functions of SPINT2 is to inhibit the Hepatocyte Growth Factor (HGF) activator, thereby preventing the formation of active HGF . This inhibition is significant because HGF is involved in various cellular processes, including growth, motility, and morphogenesis.

SPINT2 is considered a putative tumor suppressor . Mutations in the SPINT2 gene have been linked to congenital sodium diarrhea, a rare genetic disorder . The protein’s ability to inhibit serine proteases and HGF activator suggests its potential role in regulating cellular processes that, when dysregulated, can lead to tumorigenesis.

The recombinant SPINT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain. It is expressed with a 6 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques . The recombinant protein is typically formulated in a phosphate-buffered saline solution with 10% glycerol for stability . It is recommended to store the protein at 4°C for short-term use and at -20°C for long-term storage, with the addition of a carrier protein to prevent degradation .

SPINT2 is primarily used in laboratory research to study its inhibitory effects on serine proteases and its role as a tumor suppressor. Its recombinant form allows for detailed biochemical and structural studies, which can provide insights into its mechanisms of action and potential therapeutic applications.